Structure of PDB 3l4d Chain A

Receptor sequence
>3l4dA (length=448) Species: 5671 (Leishmania infantum) [Search protein sequence]
GKLPPVVHGTTPFVGHIIQFGKDPLGFMLKAKKKYGGIFTMNICGNRITV
VGDVHQHSKFFTPRNEILSPREVYSFMVPVFGEGVAYAAPYPRMREQLNF
LAEELTVAKFQNFAPSIQHEVRKFMKANWNKDEGEINILDDCSAMIINTA
CQCLFGEDLRKRLDARQFAQLLAKMESCLIPAAVFLPWILKLPLPQSYRC
RDARAELQDILSEIIIAREKEEAQKDTNTSDLLAGLLGAVYRDGTRMSQH
EVCGMIVAAMFAGQHTSTITTTWSLLHLMDPRNKRHLAKLHQEIDEFPAQ
LNYDNVMEEMPFAEQCARESIRRDPPLVMLMRKVLKPVQVGKYVVPEGDI
IACSPLLSHQDEEAFPNPREWNPERNMKLVDGAFCGFGAGVHKCIGEKFG
LLQVKTVLATVLRDYDFELLGPLPEPNYHTMVVGPTASQCRVKYIKKK
3D structure
PDB3l4d Substrate Preferences and Catalytic Parameters Determined by Structural Characteristics of Sterol 14{alpha}-Demethylase (CYP51) from Leishmania infantum.
ChainA
Resolution2.75 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) L355 C422
Catalytic site (residue number reindexed from 1) L327 C394
Enzyme Commision number 1.14.13.70: Transferred entry: 1.14.14.154.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A Y102 Y115 L126 A287 A290 G291 T294 L358 R360 G414 F415 G416 H420 C422 I423 G424 G428 Y74 Y87 L98 A259 A262 G263 T266 L330 R332 G386 F387 G388 H392 C394 I395 G396 G400
BS02 TPF A F109 Y115 A286 F289 A290 T294 L355 F81 Y87 A258 F261 A262 T266 L327
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3l4d, PDBe:3l4d, PDBj:3l4d
PDBsum3l4d
PubMed21632531
UniProtA2TEF2

[Back to BioLiP]